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RPOA_ARATH
ID   RPOA_ARATH              Reviewed;         329 AA.
AC   P56762;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=DNA-directed RNA polymerase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059};
DE            Short=PEP {ECO:0000255|HAMAP-Rule:MF_00059};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00059};
DE   AltName: Full=Plastid-encoded RNA polymerase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059};
DE            Short=RNA polymerase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059};
GN   Name=rpoA {ECO:0000255|HAMAP-Rule:MF_00059}; OrderedLocusNames=AtCg00740;
OS   Arabidopsis thaliana (Mouse-ear cress).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10574454; DOI=10.1093/dnares/6.5.283;
RA   Sato S., Nakamura Y., Kaneko T., Asamizu E., Tabata S.;
RT   "Complete structure of the chloroplast genome of Arabidopsis thaliana.";
RL   DNA Res. 6:283-290(1999).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC       {ECO:0000255|HAMAP-Rule:MF_00059}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC         EC=2.7.7.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00059};
CC   -!- SUBUNIT: In plastids the minimal PEP RNA polymerase catalytic core is
CC       composed of four subunits: alpha, beta, beta', and beta''. When a
CC       (nuclear-encoded) sigma factor is associated with the core the
CC       holoenzyme is formed, which can initiate transcription.
CC       {ECO:0000255|HAMAP-Rule:MF_00059}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- DOMAIN: The N-terminal domain is essential for RNAP assembly and basal
CC       transcription, whereas the C-terminal domain is involved in interaction
CC       with transcriptional regulators and with upstream promoter elements.
CC       {ECO:0000255|HAMAP-Rule:MF_00059}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00059}.
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DR   EMBL; AP000423; BAA84417.1; -; Genomic_DNA.
DR   RefSeq; NP_051090.1; NC_000932.1.
DR   AlphaFoldDB; P56762; -.
DR   SMR; P56762; -.
DR   BioGRID; 29933; 24.
DR   IntAct; P56762; 1.
DR   MINT; P56762; -.
DR   STRING; 3702.ATCG00740.1; -.
DR   PaxDb; P56762; -.
DR   PRIDE; P56762; -.
DR   ProteomicsDB; 226920; -.
DR   EnsemblPlants; ATCG00740.1; ATCG00740.1; ATCG00740.
DR   GeneID; 844727; -.
DR   Gramene; ATCG00740.1; ATCG00740.1; ATCG00740.
DR   KEGG; ath:ArthCp055; -.
DR   Araport; ATCG00740; -.
DR   TAIR; locus:504954697; ATCG00740.
DR   eggNOG; ENOG502QRS7; Eukaryota.
DR   HOGENOM; CLU_053084_2_0_1; -.
DR   InParanoid; P56762; -.
DR   OMA; LMKFRNF; -.
DR   OrthoDB; 990306at2759; -.
DR   PRO; PR:P56762; -.
DR   Proteomes; UP000006548; Chloroplast.
DR   ExpressionAtlas; P56762; baseline and differential.
DR   Genevisible; P56762; AT.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0042644; C:chloroplast nucleoid; HDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.170.120.12; -; 1.
DR   Gene3D; 3.30.1360.10; -; 1.
DR   HAMAP; MF_00059; RNApol_bact_RpoA; 1.
DR   InterPro; IPR011262; DNA-dir_RNA_pol_insert.
DR   InterPro; IPR011263; DNA-dir_RNA_pol_RpoA/D/Rpb3.
DR   InterPro; IPR011773; DNA-dir_RpoA.
DR   InterPro; IPR036603; RBP11-like.
DR   InterPro; IPR011260; RNAP_asu_C.
DR   InterPro; IPR036643; RNApol_insert_sf.
DR   PANTHER; PTHR32108; PTHR32108; 1.
DR   Pfam; PF01000; RNA_pol_A_bac; 1.
DR   Pfam; PF03118; RNA_pol_A_CTD; 1.
DR   Pfam; PF01193; RNA_pol_L; 1.
DR   SMART; SM00662; RPOLD; 1.
DR   SUPFAM; SSF55257; SSF55257; 1.
DR   SUPFAM; SSF56553; SSF56553; 1.
DR   TIGRFAMs; TIGR02027; rpoA; 1.
PE   3: Inferred from homology;
KW   Chloroplast; DNA-directed RNA polymerase; Nucleotidyltransferase; Plastid;
KW   Reference proteome; Transcription; Transferase.
FT   CHAIN           1..329
FT                   /note="DNA-directed RNA polymerase subunit alpha"
FT                   /id="PRO_0000175440"
FT   REGION          1..233
FT                   /note="Alpha N-terminal domain (alpha-NTD)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
FT   REGION          266..329
FT                   /note="Alpha C-terminal domain (alpha-CTD)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00059"
SQ   SEQUENCE   329 AA;  38137 MW;  A7893F7C7C70D981 CRC64;
     MVREKVKVST RTLQWKCVES KRDSKRLYYG RFILSPLMKG QADTIGIAMR RALLGEIEGT
     CITRAKSENI PHDYSNIAGI QESVHEILMN LNEIVLRSNL YGTRNALICV QGPGYITARD
     IILPPAVEII DNTQHIATLT EPIDLCIELK IERNRGYSLK MSNNFEDRSY PIDAVFMPVE
     NANHSIHSYG NGNEKQEILF LEIWTNGSLT PKEALHQASR NLINLFIPFL HVEEETFYLE
     NNQHQVTLPF FPFHNRLVNL RKKKKTKELA FQYIFIDQLE LPPRIYNCLK KSNIHTLLDL
     LNNSQEDLIK IEHFHVEDVK KILDILEKK
 
 
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